Structure of PDB 6fja Chain A Binding Site BS02

Receptor Information
>6fja Chain A (length=455) Species: 329 (Ralstonia pickettii) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
LPGDFGPPRGEPIHAVLTSPPLVPPPVNRTYPAKVIVELEVVEKEMQISE
GVSYTFWTFGGTVPGSFIRVRQGDTVEFHLKNHPSSKMPHNIDLHGVTGP
GGGAASSFTAPGHESQFTFKALNEGIYVYHCATAPVGMHIANGMYGLILV
EPPEGLPKVDHEYYVMQGDFYTAGKYREKGLQPFDMEKAIDERPSYVLFN
GAEGALTGDKALHAKVGETVRIFVGNGGPNLVSSFHVIGAIFDQVRYEGG
TNVQKNVQTTLIPAGGAAVVKFTARVPGSYVLVDHSIFRAFNKGAMAILK
IDGAENKLVYSGKELDSVYLGDRAAPNMSAVTKATQASVSGTLTVQDQVQ
AGRALFAGTCSVCHQGNGAGLPGVFPPLAKSDFLAADPKRAMNIVLHGLN
GKIKVNGQEYDSVMPPMTQLNDDEVANILTYVLNSWDNPGGRVSAEDVKK
VRAQP
Ligand information
Ligand IDHEM
InChIInChI=1S/C34H34N4O4.Fe/c1-7-21-17(3)25-13-26-19(5)23(9-11-33(39)40)31(37-26)16-32-24(10-12-34(41)42)20(6)28(38-32)15-30-22(8-2)18(4)27(36-30)14-29(21)35-25;/h7-8,13-16H,1-2,9-12H2,3-6H3,(H4,35,36,37,38,39,40,41,42);/q;+2/p-2/b25-13-,26-13-,27-14-,28-15-,29-14-,30-15-,31-16-,32-16-;
InChIKeyKABFMIBPWCXCRK-RGGAHWMASA-L
SMILES
SoftwareSMILES
OpenEye OEToolkits 1.7.6Cc1c2n3c(c1CCC(=O)O)C=C4C(=C(C5=[N]4[Fe]36[N]7=C(C=C8N6C(=C5)C(=C8C)C=C)C(=C(C7=C2)C)C=C)C)CCC(=O)O
CACTVS 3.385CC1=C(CCC(O)=O)C2=Cc3n4[Fe]5|6|N2=C1C=c7n5c(=CC8=N|6C(=Cc4c(C)c3CCC(O)=O)C(=C8C=C)C)c(C)c7C=C
ACDLabs 12.01C=1c3c(c(c4C=C5C(=C(C=6C=C7C(=C(C8=CC=2C(=C(C=1N=2[Fe](n34)(N5=6)N78)CCC(=O)O)C)\C=C)C)\C=C)C)C)CCC(=O)O
FormulaC34 H32 Fe N4 O4
NamePROTOPORPHYRIN IX CONTAINING FE;
HEME
ChEMBL
DrugBankDB18267
ZINC
PDB chain6fja Chain A Residue 502 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

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PDB6fja Activation of redox tyrosine switch is required for ligand binding at the catalytic site in heme-cu nitrite reductases
Resolution2.2 Å
Binding residue
(original residue number in PDB)		T363 C364 C367 H368 P380 P381 L382 F387 N404 G405 Y414 S416 M418 M421
Binding residue
(residue number reindexed from 1)		T359 C360 C363 H364 P376 P377 L378 F383 N400 G401 Y410 S412 M414 M417
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) H94 D97 H99 H134 C135 H143 M148 H240 Q262 T263 H289
Catalytic site (residue number reindexed from 1) H90 D93 H95 H130 C131 H139 M144 H236 Q258 T259 H285
Enzyme Commision number 1.7.2.1: nitrite reductase (NO-forming).
Gene Ontology
Molecular Function
GO:0005507 copper ion binding
GO:0009055 electron transfer activity
GO:0016491 oxidoreductase activity
GO:0020037 heme binding
GO:0046872 metal ion binding
GO:0050421 nitrite reductase (NO-forming) activity
Cellular Component
GO:0042597 periplasmic space

View graph for
Molecular Function
View graph for
Cellular Component
External links
PDB RCSB:6fja, PDBe:6fja, PDBj:6fja
PDBsum6fja
PubMed
UniProtI6NAW4

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